Preparation and Characterization of Highly Flexible, Free‐Standing, Three‐Dimensional and Rough NiMOF/rGO Composite Paper Electrode for Determination of Catechol

2019 ◽  
Vol 4 (21) ◽  
pp. 6488-6495 ◽  
Author(s):  
Kader Dağcı Kıranşan
2000 ◽  
Vol 33 (4) ◽  
pp. 1023-1030 ◽  
Author(s):  
M. Ohler ◽  
M. Sanchez del Rio ◽  
A. Tuffanelli ◽  
M. Gambaccini ◽  
A. Taibi ◽  
...  

Section topographs recorded at different spatial locations and at different rocking angles of a highly oriented pyrolytic graphite (HOPG) crystal allow three-dimensional maps of the local angular-dependent scattering power to be obtained. This is performed with a direct reconstruction from the intensity distribution on such topographs. The maps allow the extraction of information on local structural parameters such as size, form and internal mosaic spread of crystalline domains. This data analysis leads to a new method for the characterization of mosaic crystals. Perspectives and limits of applicability of this method are discussed.


2018 ◽  
Vol 20 (42) ◽  
pp. 27059-27068 ◽  
Author(s):  
Hossein Eslami ◽  
Parvin Sedaghat ◽  
Florian Müller-Plathe

Local order parameters for the characterization of liquid and different two- and three-dimensional crystalline structures are presented.


2020 ◽  
Vol 12 (45) ◽  
pp. 5476-5484
Author(s):  
Maren Christin Stillesby Levernæs ◽  
Arelí Urtubia Moe ◽  
Sigurd Leinæs Bøe ◽  
Elisabeth Paus ◽  
Léon Reubsaet ◽  
...  

Here we evaluate a quick and easy tool for determination of epitope configuration using immunocapture and liquid chromatography mass spectrometry (LC-MS) subsequent to pre-treatment of the target protein to disrupt its three-dimensional structure.


2013 ◽  
Author(s):  
◽  
Richa Dhatwalia

UDP-galactopyranose mutase (UGM) is a unique flavoenzyme that catalyzes the interconversion between UDP-galactopyranose (UDP-Galp) and UDP-galactofuranose (UDP-Galf), without any net transfer of electrons. UGM is a central enzyme involved in the biosynthesis of galactofuranose (Galf). Galf forms a major component of different glycoconjugate structures, lipids and polysaccharides of disease-causing fungi, Aspergillus fumigatus and protozoan parasites such as Trypanosoma cruzi and Leishmania major. Current treatments for diseases caused by these pathogens are limited and use compounds that are either highly toxic or expensive. Thus, new drug development strategies are required for combating these lethal diseases. The unique chemistry of UGMs and its implication in the virulence of pathogenic bacteria, fungi and protozoa and its absence in humans make it a potential drug target. Though bacterial UGMs have been somewhat characterized in detail using structural and biochemical methods, major questions about the catalytic and structural properties of eukaryotic UGMs remain unanswered. Thus, the determination of three-dimensional structures of eukaryotic UGMs might help us in elucidating the enzymatic mechanism of this class of enzymes and potential inhibitor design. The research described in this dissertation address these longstanding questions by providing the first three-dimensional structural details and biochemical characterization of eukaryotic UGMs.


2006 ◽  
Vol 39 (1) ◽  
pp. 106-108 ◽  
Author(s):  
J. M. Yi ◽  
Y. S. Chu ◽  
T. S. Argunova ◽  
J. H. Je

A technique, using a symmetric reflectionviaazimuthal rotation of a sample, is presented for characterization of the three-dimensional distribution of dislocations in single crystals. An analytic formula is derived to transform the three-dimensional geometry of a straight dislocation into its two-dimensional projection onto the detector plane. By fitting topographs to the formula, the orientations and locations of dislocations are quantitatively determined. The dislocations in a thermally stressed Si wafer are examined as an example.


1985 ◽  
Vol 22 (01) ◽  
pp. 82-98 ◽  
Author(s):  
E. B. Jensen ◽  
H. J. G. Gundersen

In stereology or applied geometric probability quantitative characterization of aggregates of particles from information on lower-dimensional sections plays a major role. Most stereological methods developed for particle aggregates are based on the assumption that the particles are of the same, known (simple) shape. Information on the volume-weighted distribution of particle size may, however, be obtained under fairly general assumptions about particle shape if particle volume is chosen as size parameter. In fact, there exists in this case an unbiased stereological estimator of the first moment under the sole assumption that the particles are convex. In the present paper, we consider a particle aggregate in ℝ and derive estimators of the q th moment of the volume-weighted distribution of particle volume, based on point-sampling of particles and measurements on q -flats through sampled particles. The estimators are valid for arbitrarily shaped particles but if the particles are non-convex it is necessary for the determination of the estimators to be able to identify the different separated parts on a q-flat through the particle aggregate which belong to the same particle. Explicit forms of the estimators are given for q = 1. For q = 2, an explicit form of one of the estimators is derived for an aggregate of triaxial ellipsoids in three-dimensional space.


1985 ◽  
Vol 22 (1) ◽  
pp. 82-98 ◽  
Author(s):  
E. B. Jensen ◽  
H. J. G. Gundersen

In stereology or applied geometric probability quantitative characterization of aggregates of particles from information on lower-dimensional sections plays a major role. Most stereological methods developed for particle aggregates are based on the assumption that the particles are of the same, known (simple) shape. Information on the volume-weighted distribution of particle size may, however, be obtained under fairly general assumptions about particle shape if particle volume is chosen as size parameter. In fact, there exists in this case an unbiased stereological estimator of the first moment under the sole assumption that the particles are convex. In the present paper, we consider a particle aggregate in ℝ and derive estimators of the q th moment of the volume-weighted distribution of particle volume, based on point-sampling of particles and measurements on q -flats through sampled particles. The estimators are valid for arbitrarily shaped particles but if the particles are non-convex it is necessary for the determination of the estimators to be able to identify the different separated parts on a q-flat through the particle aggregate which belong to the same particle. Explicit forms of the estimators are given for q = 1. For q = 2, an explicit form of one of the estimators is derived for an aggregate of triaxial ellipsoids in three-dimensional space.


2019 ◽  
Vol 52 (3) ◽  
pp. 571-578 ◽  
Author(s):  
Y. Chushkin ◽  
F. Zontone ◽  
O. Cherkas ◽  
A. Gibaud

This article presents a combined approach where quantitative forward-scattering coherent diffraction imaging (CDI) is supported by crystal diffraction using 8.1 keV synchrotron X-ray radiation. The method allows the determination of the morphology, mass density and crystallinity of an isolated microscopic specimen. This approach is tested on three homogeneous samples made of different materials with different degrees of crystallinity. The mass density and morphology are revealed using three-dimensional coherent diffraction imaging with a resolution better than 36 nm. The crystallinity is extracted from the diffraction profiles measured simultaneously with coherent diffraction patterns. The presented approach extends CDI to structural characterization of samples when crystallinity aspects are of interest.


1991 ◽  
Vol 24 (3) ◽  
pp. 227-291 ◽  
Author(s):  
J. C. Smith

To deepen our understanding of the principles determining the folding and functioning of globular proteins the determination of their three-dimensional structures must be supplemented with the characterization of their internal motions. Although dynamical events in proteins occur on time-scale ranging from femtoseconds to at least seconds, the physical properties of globular proteins are such that picosecond (ps) time-scale motions make a particularly important contribution to the internal fluctuations of the atoms from their mean positions.


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